Caldolase, a chelator-insensitive extracellular serine proteinase from a Thermus spp
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چکیده
منابع مشابه
Processing of the lactococcal extracellular serine proteinase.
Activity of the lactococcal cell envelope-located serine proteinase depends on the presence of membrane-associated lipoprotein PrtM. To differentiate between the action of the proteinase and the action of PrtM in the process of proteinase maturation, an inactive form of the lactococcal proteinase was constructed. This was done by mutating one of the three amino acids thought to constitute the a...
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An extracellular proteinase was purified from culture filtrates of Cryptococcus neoformans NHPY24 by DEAE ion-exchange chromatography and gelatin affinity column chromatography with azoalbumin as the substrate. The molecular mass of the purified enzyme was 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, its pH optimum was 7.0 to 8.0, and maximal activity was obtained at pH ...
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The serine proteinase isolated from Thermomonospora fusca YX shows considerable thermal stability up to 80 °C, and progressive inactivation occurs at higher temperatures. Lyotropic salts affected the thermal stability of the enzyme at 85 °C, suggesting that disruption of hydrophobic interactions play an important role in the decreased thermal stability of the enzyme above 80 'C. Thermal stabili...
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An extracellular proteinase produced by the filamentous fungus Scedosporium apiospermum has been purified and characterized. Initially, in vitro conditions for enzyme synthesis were investigated. The highest yield of enzyme production was obtained when the fungus was cultivated in modified Czapek-Dox liquid medium supplemented with 0.1% bacteriological peptone and 1% (w/v) glucose as the nitrog...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1989
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2620409